9512492

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0013138, umls-concept:C0076919, umls-concept:C0212320, umls-concept:C0439855, umls-concept:C0449432, umls-concept:C0526260, umls-concept:C1179435, umls-concept:C1428360, umls-concept:C1514562, umls-concept:C1524073, umls-concept:C1548799, umls-concept:C1705248, umls-concept:C1879547, umls-concept:C1880389, umls-concept:C1883204, umls-concept:C1883221
pubmed:dateCreated	1998-5-13
pubmed:abstractText	The CCAAT-binding factor CBF is a heterotrimeric transcription factor that specifically binds to CCAAT sequences in many eukaryotic genes. Previous studies have shown that CBF contains two transcription activation domains: a glutamine-rich, serine-threonine-rich domain present in the CBF-B subunit and a glutamine-rich domain in the CBF-C subunit. In this study, by using a series of deletion mutations of CBF-B and CBF-C in transcription assay in vitro, we further delineated smaller segments in these domains that were sufficient to support transcriptional activation by CBF. To test whether transcription activation by CBF requires co-activators, we examined the interaction between CBF and dTAF110, a component of the Drosophila TFIID complex. Recent work has demonstrated that glutamine-rich domains of the Sp1 transcription factor interact with dTAF110 and that this interaction has an important role in mediating transcription activation. Here we first demonstrate in a direct interaction assay in vitro that CBF binds dTAF110. By using a yeast two-hybrid system we show that both of the transcription activation domains of CBF interact with dTAF110. A deletion analysis suggests that a segment of CBF-B needed for transcription activation is also involved in interaction with dTAF110. In CBF-C the C-terminal portion of the molecule seems to be needed for these two activities. Our results suggest that TAF110 might represent one of the co-activators that mediate transcriptional activation by CBF.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/AR 43660, http://linkedlifedata.com/resource/pubmed/grant/CA 16672, http://linkedlifedata.com/resource/pubmed/grant/CA 49515
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2984726R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Core Binding Factors, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TATA-Binding Protein Associated..., http://linkedlifedata.com/resource/pubmed/chemical/Taf4 protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIID, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	0264-6021
pubmed:author	pubmed-author:CoustryFF, pubmed-author:CrombruggheBB, pubmed-author:MaityS NSN, pubmed-author:SinhaSS
pubmed:issnType	Print
pubmed:day	1
pubmed:volume	331 ( Pt 1)
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	291-7
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:9512492-Animals, pubmed-meshheading:9512492-Binding Sites, pubmed-meshheading:9512492-Core Binding Factors, pubmed-meshheading:9512492-DNA-Binding Proteins, pubmed-meshheading:9512492-Drosophila, pubmed-meshheading:9512492-Drosophila Proteins, pubmed-meshheading:9512492-Neoplasm Proteins, pubmed-meshheading:9512492-Protein Binding, pubmed-meshheading:9512492-TATA-Binding Protein Associated Factors, pubmed-meshheading:9512492-Transcription Factor TFIID, pubmed-meshheading:9512492-Transcription Factors, pubmed-meshheading:9512492-Transcription Factors, TFII
pubmed:year	1998
pubmed:articleTitle	The two activation domains of the CCAAT-binding factor CBF interact with the dTAFII110 component of the Drosophila TFIID complex.
pubmed:affiliation	Department of Molecular Genetics, The University of Texas, M.D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX77030, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S.